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Escherichia coli K-12 substr. MG1655 Reaction: 4.1.2.5/4.1.2.48

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 4.1.2.5 , 4.1.2.48

Enzymes and Genes:
low-specificity L-threonine aldolase Inferred from experiment : ltaE

In Pathway: threonine degradation IV

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: Balanced.

Enzyme Commission Primary Name for 4.1.2.5: L-threonine aldolase

Enzyme Commission Synonyms for 4.1.2.5: L-threonine acetaldehyde-lyase

Enzyme Commission Primary Name for 4.1.2.48: low-specificity L-threonine aldolase

Enzyme Commission Synonyms for 4.1.2.48: LtaE

Enzyme Commission Summary for 4.1.2.5:
A pyridoxal-phosphate protein. This enzyme is specific for L-threonine and can not utilize L-allo-threonine. Different from EC 4.1.2.49, L-allo-threonine aldolase, and EC 4.1.2.48, low-specificity L-threonine aldolase.

Enzyme Commission Summary for 4.1.2.48:
Requires pyridoxal phosphate. The low-specificity L-threonine aldolase can act on both L-threonine and L-allo-threonine [Yamada70, Kumagai72]. The enzyme from Escherichia coli can also act on L-threo-phenylserine and L-erythro-phenylserine [Liu98d]. The enzyme can also catalyse the aldol condensation of glycolaldehyde and glycine to form 4-hydroxy-L-threonine, an intermediate of pyridoxal phosphate biosynthesis [Liu97c]. Different from EC 4.1.2.5, L-threonine aldolase, and EC 4.1.2.49, L-allo-threonine aldolase.

Citations: [Dainty70, Karasek57, Kim10a]

Gene-Reaction Schematic: ?

Instance reaction of [DL-allothreonine ↔ acetaldehyde + glycine] (4.1.2.-):
i1: L-allo-threonine ↔ glycine + acetaldehyde (4.1.2.48/4.1.2.49)

Relationship Links: BRENDA:EC:4.1.2.5 , BRENDA:EC:4.1.2.48 , ENZYME:EC:4.1.2.5 , ENZYME:EC:4.1.2.48 , IUBMB-ExplorEnz:EC:4.1.2.5 , IUBMB-ExplorEnz:EC:4.1.2.48


References

Dainty70: Dainty RH (1970). "Purification and properties of threonine aldolase from Clostridium pasteurianum." Biochem J 117(3);585-92. PMID: 5419751

Karasek57: Karasek MA, Greenberg DM (1957). "Studies on the properties of threonine aldolases." J Biol Chem 227(1);191-205. PMID: 13449064

Kim10a: Kim J, Kershner JP, Novikov Y, Shoemaker RK, Copley SD (2010). "Three serendipitous pathways in E. coli can bypass a block in pyridoxal-5'-phosphate synthesis." Mol Syst Biol 6;436. PMID: 21119630

Kumagai72: Kumagai H, Nagate T, Yoshida H, Yamada H (1972). "Threonine aldolase from Candida humicola. II. Purification, crystallization and properties." Biochim Biophys Acta 258(3);779-90. PMID: 5017702

Liu97c: Liu JQ, Nagata S, Dairi T, Misono H, Shimizu S, Yamada H (1997). "The GLY1 gene of Saccharomyces cerevisiae encodes a low-specific L-threonine aldolase that catalyzes cleavage of L-allo-threonine and L-threonine to glycine--expression of the gene in Escherichia coli and purification and characterization of the enzyme." Eur J Biochem 245(2);289-93. PMID: 9151955

Liu98d: Liu JQ, Dairi T, Itoh N, Kataoka M, Shimizu S, Yamada H (1998). "Gene cloning, biochemical characterization and physiological role of a thermostable low-specificity L-threonine aldolase from Escherichia coli." Eur J Biochem 1998;255(1);220-6. PMID: 9692922

Yamada70: Yamada H, Kumagai H, Nagate T, Yoshida H (1970). "Crystalline threonine aldolase from Candida humicola." Biochem Biophys Res Commun 39(1);53-8. PMID: 5438301


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Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Mon Dec 22, 2014, biocyc13.